Translational Repression in Bacteriophage F1: Characterization of the Gene V Protein Target on the Gene II mRNA

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 86; no. 11; pp. 4002 - 4006
• Main Authors: Michel, Benedicte, Zinder, Norton D.
• Format: Journal Article
• Language: English
• Published: Washington, DC National Academy of Sciences of the United States of America 01.06.1989; National Acad Sciences
• Subjects: Bacteriophages; Base Sequence; Biological and medical sciences; Coliphages - genetics; DNA; Escherichia coli - genetics; Five prime untranslated regions; Fundamental and applied biological sciences. Psychology; Gene Expression Regulation; Genes; Genes, Viral; Genetic mutation; Messenger RNA; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Mutation; Nucleotides; Plasmids; Protein Biosynthesis; Replication origin; Repression; RNA; RNA, Messenger - genetics; Translation. Translation factors. Protein processing; Viral Proteins - genetics; Phage f1; Site directed mutagenesis; DNA binding protein; Molecular interaction; Translation repressor; Virus; Characterization; Proteins; Target; Messenger RNA; Structure activity relation; Hybrid gene; Phage
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.86.11.4002

Previous studies have shown that the single-stranded DNA binding protein of bacteriophage f1 (gene V protein) represses the translation of the mRNA of the phage-encoded replication protein (gene II protein). We have characterized phage mutations in the repressor and in its target. Using a gene II-lacZ translational fusion, we have defined a 16-nucleotide-long region in the gene II mRNA sequence that is required in vivo for repression by the gene V protein. We have shown that in vitro the binding affinity of the gene V protein is at least 10-fold higher to an RNA carrying this sequence than to an RNA lacking it. We propose that this sequence constitutes the gene II mRNA operator.